Crystals of DhaA Mutants from Rhodococcus rhodochrous NCIMB 13064 Diffracted to Ultrahigh Resolution: Crystallization and Preliminary Diffraction Analysis

Authors

Stsiapanava, A., Koudelakova, T., Lapkouski, M., Pavlova, M., Damborsky, J., Kuta Smatanova, I.

Source

ACTA CRYSTALLOGRAPHICA F64: 137-140 (2008)

Abstract

The enzyme DhaA from Rhodococcus rhodochrous NCIMB 13064 belongs to the haloalkane dehalogenases, which catalyze the hydrolysis of haloalkanes to the corresponding alcohols. The haloalkane dehalogenase DhaA and its variants can be used to detoxify the industrial pollutant 1,2,3-trichloropropane (TCP). Three mutants named DhaA04, DhaA14 and DhaA15 were constructed in order to study the importance of tunnels connecting the buried active site with the surrounding solvent to the enzymatic activity. All protein mutants were crystallized using the sitting-drop vapour-diffusion method. The crystals of DhaA04 belonged to the orthorhombic space group P212121, while the crystals of the other two mutants DhaA14 and DhaA15 belonged to the triclinic space group P1. Native data sets were collected for the DhaA04, DhaA14 and DhaA15 mutants at beamline X11 of EMBL, DESY, Hamburg to the high resolutions of 1.30, 0.95 and 1.15 Å, respectively.

Full text

Citation

Stsiapanava, A., Koudelakova, T., Lapkouski, M., Pavlova, M., Damborsky, J., Kuta Smatanova, I., 2008: Crystals of DhaA Mutants from Rhodococcus rhodochrous NCIMB 13064 Diffracted to Ultrahigh Resolution: Crystallization and Preliminary Diffraction Analysis. Acta Crystallographica F64: 137-140.

Marie Curie Grants for Piia and Stas
A Marie Curie Grant for Martin Marek
Sergio Marques the Most Ardent Journal Reader
Summer School of Protein Engineering
Prof. Donald Hilvert to Give Lectute at Masaryk University
Zbynek Prokop’s Professorship Approved by the President
Open Postdoc Position: Protein Engineering